PEPT2_CAEEL
ID PEPT2_CAEEL Reviewed; 785 AA.
AC Q17758; O76185;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 27-MAY-2002, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Peptide transporter family 2;
DE AltName: Full=Di-/tri-peptide transporter CPTA;
DE AltName: Full=Oligopeptide transporter 1;
GN Name=pept-2; Synonyms=cpta, opt-1, pep-1; ORFNames=C06G8.2;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE.
RC STRAIN=Bristol N2;
RX PubMed=9601088; DOI=10.1042/bj3320565;
RA Fei Y.-J., Fujita T., Lapp D.F., Ganapathy V., Leibach F.H.;
RT "Two oligopeptide transporters from Caenorhabditis elegans: molecular
RT cloning and functional expression.";
RL Biochem. J. 332:565-572(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP TISSUE SPECIFICITY.
RX PubMed=12939266; DOI=10.1074/jbc.m307351200;
RA Nehrke K.;
RT "A reduction in intestinal cell pHi due to loss of the Caenorhabditis
RT elegans Na+/H+ exchanger NHX-2 increases life span.";
RL J. Biol. Chem. 278:44657-44666(2003).
RN [4]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-467, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=Bristol N2;
RX PubMed=17761667; DOI=10.1074/mcp.m600392-mcp200;
RA Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T.,
RA Taoka M., Takahashi N., Isobe T.;
RT "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis
RT elegans and suggests an atypical translocation mechanism for integral
RT membrane proteins.";
RL Mol. Cell. Proteomics 6:2100-2109(2007).
CC -!- FUNCTION: Proton-dependent uptake of di- or tripeptides, and to a minor
CC extent tetrapeptides. Transport is independent of sodium and chloride
CC ions. Protein shows high affinity to peptide substrates.
CC {ECO:0000269|PubMed:9601088}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Expressed in vulval, pharyngeal and anal muscles.
CC {ECO:0000269|PubMed:12939266}.
CC -!- DEVELOPMENTAL STAGE: Gradual increase in expression during development
CC from embryo through to adult with highest levels of expression in the
CC late larval and adult stages. {ECO:0000269|PubMed:9601088}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Proton-
CC dependent oligopeptide transporter (POT/PTR) (TC 2.A.17) family.
CC {ECO:0000305}.
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DR EMBL; AF000417; AAC39118.1; -; mRNA.
DR EMBL; Z70306; CAA94323.2; -; Genomic_DNA.
DR PIR; T19017; T19017.
DR PIR; T37329; T37329.
DR RefSeq; NP_502002.1; NM_069601.3.
DR AlphaFoldDB; Q17758; -.
DR SMR; Q17758; -.
DR STRING; 6239.C06G8.2; -.
DR TCDB; 2.A.17.4.3; the proton-dependent oligopeptide transporter (pot/ptr) family.
DR iPTMnet; Q17758; -.
DR EPD; Q17758; -.
DR PaxDb; Q17758; -.
DR PeptideAtlas; Q17758; -.
DR EnsemblMetazoa; C06G8.2.1; C06G8.2.1; WBGene00003876.
DR GeneID; 177973; -.
DR KEGG; cel:CELE_C06G8.2; -.
DR UCSC; C06G8.2; c. elegans.
DR CTD; 177973; -.
DR WormBase; C06G8.2; CE28887; WBGene00003876; pept-2.
DR eggNOG; KOG1237; Eukaryota.
DR HOGENOM; CLU_004790_3_0_1; -.
DR InParanoid; Q17758; -.
DR OMA; CHNRVSI; -.
DR OrthoDB; 365203at2759; -.
DR PhylomeDB; Q17758; -.
DR Reactome; R-CEL-427975; Proton/oligopeptide cotransporters.
DR PRO; PR:Q17758; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00003876; Expressed in adult organism and 3 other tissues.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0071916; F:dipeptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR036259; MFS_trans_sf.
DR InterPro; IPR004768; Oligopep_transport.
DR InterPro; IPR000109; POT_fam.
DR InterPro; IPR018456; PTR2_symporter_CS.
DR PANTHER; PTHR11654; PTHR11654; 1.
DR Pfam; PF00854; PTR2; 2.
DR SUPFAM; SSF103473; SSF103473; 1.
DR TIGRFAMs; TIGR00926; 2A1704; 1.
DR PROSITE; PS01022; PTR2_1; 1.
DR PROSITE; PS01023; PTR2_2; 1.
PE 1: Evidence at protein level;
KW Glycoprotein; Membrane; Peptide transport; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..785
FT /note="Peptide transporter family 2"
FT /id="PRO_0000064313"
FT TRANSMEM 46..66
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 99..119
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 134..154
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..365
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 670..690
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 711..731
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CARBOHYD 467
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17761667"
FT CONFLICT 483
FT /note="E -> K (in Ref. 1; AAC39118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 785 AA; 87567 MW; ED20BD106732CB77 CRC64;
MGASHLHDDP RPGSPVDHQP TTWGGIIKKW PKQTFLIVGN ELCERFSFYG MRAVLTLYFF
NILNFSQSFS TVLFHAFTVI CYSSPLLGSI LADGYIGKFW TIFFISIFYA CGQILLAFSS
IAPSGSSHHP LLDLLGLLIV GLGTGGIKPC VSAFGGDQFP AHYTRMISLF FSMFYFSINA
GSLISMWLTP YFRSMSCFGH DSCYPLAFGI PAILMIVATL VFMAGSFWYK KVPPKENIIF
KVIGTITTAL RKKASSSSTH QRSHWLEYSL DGHDCALSTE CKNLHGNCAQ RRYIEDIKRL
FRVIVMMIPV PMFWALYDQQ GSTWVLQAVG MDAKVFGFEI LPDQMGVLNA FLILFFIPIF
QSIVYPTIEK LGFQMTMLRK MAGGGILTAV SFFVCGIVQL FVNPTLPYIP MANEAHLTII
NTIPSCDFNV LIDSREPFDL LRKSGIAPDD SVRKPISFTG DDFFQPNITF DNLAPNCPKF
TAEPMLAPAT SYVLTLSPNG WAYNAVRPEK PKSGKGELSM GLNLIVPCDK IPSNVTWEQC
NGTEGYSGAI ALCKVESDVI TDNNNVCDPT AKGKFYVLSN ANPLDVHDFS KKSTVTAFGR
TYSPIEMKPG TYRLFYTDDS RTHFTPLNLP PVQQDHMGGQ YLITVSTRSK NDSEVLATTE
SLVSYNRVSI LWQIPQYVIL TAGEVLFSIT GLEFAYTEAS PQLKSVVQAL WLFTTAIGDL
IVVVIFMLNI FSDVAVQMFV FGGIMLFVIF VFILLAVFYY EYADYSNESE VLTEKMIVDD
DHTRI
